2005
SGK1 activates Na+-K+-ATPase in amphibian renal epithelial cells
de la Rosa D, Gimenez I, Forbush B, Canessa CM. SGK1 activates Na+-K+-ATPase in amphibian renal epithelial cells. American Journal Of Physiology - Cell Physiology 2005, 290: c492-c498. PMID: 16192298, DOI: 10.1152/ajpcell.00556.2004.Peer-Reviewed Original ResearchConceptsRenal epithelial cellsEpithelial cellsEffects of aldosteroneCell linesActivation of ENaCGlucocorticoid-induced kinase 1Epithelial cell lineRenal epithelial cell lineAldosteroneSGK1 expressionSame cell lineSubunit abundanceSGK1Channel activityTotal proteinImportant regulatorKinase 1Tetracycline-inducible promoterActivationCellsApical membraneATPase activityPrevious studiesATPase functionChronic
1997
Diversity of the E2P Phosphoforms of Na, K‐ATPasea
FEDOSOVA N, CORNELIUS F, FORBUSH B, KLODOS I. Diversity of the E2P Phosphoforms of Na, K‐ATPasea. Annals Of The New York Academy Of Sciences 1997, 834: 386-389. PMID: 9432913, DOI: 10.1111/j.1749-6632.1997.tb52278.x.Peer-Reviewed Original ResearchEnzyme ActivationHydroxylaminesKineticsLiposomesPhosphoproteinsPhosphorylationProteolipidsSodium-Potassium-Exchanging ATPase
1994
The molecular basis of chloride transport in shark rectal gland.
Riordan J, Forbush B, Hanrahan J. The molecular basis of chloride transport in shark rectal gland. Journal Of Experimental Biology 1994, 196: 405-418. PMID: 7529818, DOI: 10.1242/jeb.196.1.405.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiological Transport, ActiveCarrier ProteinsChloride ChannelsChloridesCystic Fibrosis Transmembrane Conductance RegulatorEpitheliumHomeostasisHumansMembrane ProteinsModels, BiologicalPotassium ChannelsProtein Structure, SecondarySalt GlandSecond Messenger SystemsSharksSodium-Potassium-Chloride SymportersSodium-Potassium-Exchanging ATPaseConceptsApical Cl- channelsCl- channelsProtein kinase ACl- secretionBasolateral transport proteinsTransepithelial Cl- secretionNa+/K(+)-ATPase pumpIntracellular chloride concentrationStimulation of secretionActive Na+ extrusionBasolateral cotransporterShark rectal glandNa+/K+/2Cl- cotransporterCl- movementK+ channelsK+ exitNa+/K(+)-ATPaseApical componentParacellular flowPrimary stimulationEpithelial cellsExcellent experimental modelCotransporterCFTRRectal gland of elasmobranchsKinetic heterogeneity of phosphoenzyme of Na,K-ATPase modeled by unmixed lipid phases. Competence of the phosphointermediate.
Klodos I, Post R, Forbush B. Kinetic heterogeneity of phosphoenzyme of Na,K-ATPase modeled by unmixed lipid phases. Competence of the phosphointermediate. Journal Of Biological Chemistry 1994, 269: 1734-1743. PMID: 8294422, DOI: 10.1016/s0021-9258(17)42089-8.Peer-Reviewed Original Research
1993
Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase.
Mercer R, Biemesderfer D, Bliss D, Collins J, Forbush B. Molecular cloning and immunological characterization of the gamma polypeptide, a small protein associated with the Na,K-ATPase. Journal Of Cell Biology 1993, 121: 579-586. PMID: 8387529, PMCID: PMC2119561, DOI: 10.1083/jcb.121.3.579.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCardiac GlycosidesCattleCloning, MolecularDNAMiceMolecular Sequence DataNephronsPeptidesRatsRNA, MessengerSequence AlignmentSheepSodium-Potassium-Exchanging ATPaseConceptsNa,K-ATPaseGamma subunitK-ATPaseSmall membrane proteinsN-linked glycosylationTissue-specific fashionCardiac glycoside bindingGamma subunit mRNAGamma-specific antibodiesNorthern blot analysisHydropathy analysisSequenced proteinsNAB-ouabainMembrane proteinsGamma polypeptidesMolecular cloningGlycoside bindingSmall proteinsNephron segmentsBeta subunitSubunit mRNAAlpha subunitSubunitAmino acidsHydrophobic domains
1991
Rate-limiting steps in Na translocation by the Na/K pump.
Forbush B, Klodos I. Rate-limiting steps in Na translocation by the Na/K pump. Society Of General Physiologists Series 1991, 46: 210-25. PMID: 1653981.Peer-Reviewed Original Research
1990
Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery.
Caplan MJ, Forbush B, Palade GE, Jamieson JD. Biosynthesis of the Na,K-ATPase in Madin-Darby canine kidney cells. Activation and cell surface delivery. Journal Of Biological Chemistry 1990, 265: 3528-3534. PMID: 2154482, DOI: 10.1016/s0021-9258(19)39801-1.Peer-Reviewed Original Research
1988
Rapid 86Rb release from an occluded state of the Na,K-pump reflects the rate of dephosphorylation or dearsenylation.
Forbush B. Rapid 86Rb release from an occluded state of the Na,K-pump reflects the rate of dephosphorylation or dearsenylation. Journal Of Biological Chemistry 1988, 263: 7961-7969. PMID: 2836403, DOI: 10.1016/s0021-9258(18)68428-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsArsenatesDimethyl SulfoxideDogsHydrogen-Ion ConcentrationKidneyKineticsMagnesiumPhosphorylationRubidiumSodium ChlorideSodium-Potassium-Exchanging ATPaseTime FactorsRapid release of 45Ca from an occluded state of the Na,K-pump.
Forbush B. Rapid release of 45Ca from an occluded state of the Na,K-pump. Journal Of Biological Chemistry 1988, 263: 7970-7978. PMID: 2836404, DOI: 10.1016/s0021-9258(18)68429-7.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCalciumCells, CulturedDogsHydrogen-Ion ConcentrationKidneyKineticsPhosphatesPotassiumRubidiumSodium-Potassium-Exchanging ATPaseConceptsNa,K-pumpNa,K-ATPaseK-pumpK-ATPasePhosphorylation of Na,K-ATPaseRelease of 45CaExposure to K+Release of 86RbApparent affinityCa2+Transport sitesK+ congenerMg2+ + ATPIntracellular faceRelease of K+Simultaneous occlusionExtracellular sitesPrevent phosphorylationCa2Exposure to Mg2Extracellular faceReleaseAbsence of PiN-methylglucamineIntracellular mediumThe interaction of amines with the occluded state of the Na,K-pump.
Forbush B. The interaction of amines with the occluded state of the Na,K-pump. Journal Of Biological Chemistry 1988, 263: 7979-7988. PMID: 2836405, DOI: 10.1016/s0021-9258(18)68430-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAminesAnimalsCells, CulturedCholineDogsEthylenediaminesKidneyMagnesiumMagnesium CompoundsPhosphatesProtein ConformationQuaternary Ammonium CompoundsRubidiumSodium-Potassium-Exchanging ATPaseConceptsRelease of 86RbInteraction of aminesPresence of aminesNa,K-pumpIntracellular faceDog kidney NaK-pumpK-ATPaseEffect of aminesBenzyl amineBifunctional aminesBlock releaseKidney NaOcclusionOrganic cationsPre-incubationAminesAmine blocksTransport sitesPresence of ATPK+ siteCompetitive mannerLow affinityOccluded stateOverview: occluded ions and Na, K-ATPase.
Forbush B. Overview: occluded ions and Na, K-ATPase. Progress In Clinical And Biological Research 1988, 268A: 229-48. PMID: 2843866.Peer-Reviewed Original Research
1987
Monoclonal antibody localization of Na+-K+-ATPase in the exocrine pancreas and parotid of the dog
Smith ZD, Caplan MJ, Forbush B, Jamieson JD. Monoclonal antibody localization of Na+-K+-ATPase in the exocrine pancreas and parotid of the dog. American Journal Of Physiology 1987, 253: g99-g109. PMID: 2441610, DOI: 10.1152/ajpgi.1987.253.2.g99.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntibodies, MonoclonalDogsImmunologic TechniquesIon ChannelsMiceMice, Inbred BALB CMicroscopy, ElectronPancreasParotid GlandSodium-Potassium-Exchanging ATPaseConceptsDuct cellsAcinar cellsRenal tubular cellsInterlobular duct cellsSodium pumpMonoclonal antibody localizationDuct-derived cellsIntralobular duct cellsTubular cellsElectrolyte secretionFrozen sectionsPancreasExocrine pancreasMonoclonal antibodiesOligosaccharide determinantsParotidAntibody localizationParotid cellsAntibodiesDog pancreasThin frozen sectionsRapid release of 42K and 86Rb from an occluded state of the Na,K-pump in the presence of ATP or ADP.
Forbush B. Rapid release of 42K and 86Rb from an occluded state of the Na,K-pump in the presence of ATP or ADP. Journal Of Biological Chemistry 1987, 262: 11104-11115. PMID: 2440883, DOI: 10.1016/s0021-9258(18)60932-9.Peer-Reviewed Original ResearchRapid release of 42K or 86Rb from two distinct transport sites on the Na,K-pump in the presence of Pi or vanadate.
Forbush B. Rapid release of 42K or 86Rb from two distinct transport sites on the Na,K-pump in the presence of Pi or vanadate. Journal Of Biological Chemistry 1987, 262: 11116-11127. PMID: 2440884, DOI: 10.1016/s0021-9258(18)60933-0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsBinding SitesBiological TransportCationsDogsIon ChannelsKidneyMagnesiumPhosphatesPotassiumPotassium RadioisotopesRadioisotopesRubidiumSodiumSodium-Potassium-Exchanging ATPaseVanadatesVanadium
1985
Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments
Kashgarian M, Biemesderfer D, Caplan M, Forbush B. Monoclonal antibody to Na,K-ATPase: Immunocytochemical localization along nephron segments. Kidney International 1985, 28: 899-913. PMID: 3003443, DOI: 10.1038/ki.1985.216.Peer-Reviewed Original ResearchConceptsMonoclonal antibodiesNephron segmentsEvidence of labellingRenal tubular epithelial cellsTubular epithelial cellsK-ATPaseThick ascending limbOnly principal cellsDifferent nephron segmentsDog antigensBasal-lateral membranesSignificant antibodiesAscending limbMesangial regionHenle's loopOccasional cellsRenal medullaOuter renal medullaAbundant antibodyAntibodiesApical labelingTubule segmentsPrincipal cellsEpithelial cellsImmunocytochemical localization
1984
Na+ movement in a single turnover of the Na pump.
Forbush B. Na+ movement in a single turnover of the Na pump. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 5310-5314. PMID: 6089192, PMCID: PMC391693, DOI: 10.1073/pnas.81.17.5310.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCell MembraneDogsIntracellular MembranesKidneyKineticsMicrosomesOuabainProtein BindingSodiumSodium-Potassium-Exchanging ATPaseThermodynamicsAn apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins
Forbush B. An apparatus for rapid kinetic analysis of isotopic efflux from membrane vesicles and of ligand dissociation from membrane proteins. Analytical Biochemistry 1984, 140: 495-505. PMID: 6091496, DOI: 10.1016/0003-2697(84)90200-8.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsDogsFiltrationKidney MedullaKineticsLigandsMembrane ProteinsPhotochemistryPressureRadioisotopesSodium-Potassium-Exchanging ATPase
1983
Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin
Forbush B. Assay of Na,K-ATPase in plasma membrane preparations: Increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin. Analytical Biochemistry 1983, 128: 159-163. PMID: 6303151, DOI: 10.1016/0003-2697(83)90356-1.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBrainBuffersCell MembraneCell Membrane PermeabilityDogsEelsEnzyme ActivationKidneyMembrane ProteinsRabbitsSerum Albumin, BovineSodium Dodecyl SulfateSodium-Potassium-Exchanging ATPaseConceptsMaximal Na,K-ATPase activityAmount of membrane proteinNa,K-ATPase activityElectric organ of eelIsolated plasma membranesNa,K-ATPaseSodium dodecyl sulfate bufferK-ATPase activityPlasma membrane preparationsTransmembrane proteinsMembrane proteinsDetergent bufferPlasma membraneOptimal activityActivity of membranesBovine serum albuminMembrane vesiclesK-ATPasePermeability of membrane vesiclesDetergentDetergent activitySulfate bufferProteinVesicular natureSerum albumin
1982
Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla.
Forbush B. Characterization of right-side-out membrane vesicles rich in (Na,K)-ATPase and isolated from dog kidney outer medulla. Journal Of Biological Chemistry 1982, 257: 12678-12684. PMID: 6290476, DOI: 10.1016/s0021-9258(18)33564-6.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell MembraneDogsKidney MedullaKineticsSodium Dodecyl SulfateSodium-Potassium-Exchanging ATPaseTrypsinValinomycinConceptsDog kidney outer medullaK)-ATPase activityK)-ATPaseKidney outer medullaOuter medullaRight-side-out membrane vesiclesMembrane vesiclesBasolateral membranePorcine trypsinMg2+ + ATPRight-side-out orientationDensity gradient centrifugationCaged ATPIntravesicular volumePresence of Na+H1 populationMedullaMembrane proteinsSucrose gradientsGradient centrifugationTrypsin-sensitiveDetergent treatmentVesicle volumeVesiclesATPPurification and characterization of an (Na++K+)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain
Collins J, Forbush B, Lane L, Ling E, Schwartz A, Zot A. Purification and characterization of an (Na++K+)-ATPase proteolipid labeled with a photoaffinity derivative of ouabain. Biochimica Et Biophysica Acta 1982, 686: 7-12. PMID: 6279154, DOI: 10.1016/0005-2736(82)90145-6.Peer-Reviewed Original ResearchMeSH KeywordsAmino AcidsAnimalsKidney MedullaOuabainProtein BindingProteolipidsSheepSodium-Potassium-Exchanging ATPaseTritium